ID A0A124JZC2_9SPHN Unreviewed; 553 AA.
AC A0A124JZC2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KUR79923.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:KUR79923.1};
GN ORFNames=AQZ50_03380 {ECO:0000313|EMBL:KUR79923.1};
OS Novosphingobium sp. Fuku2-ISO-50.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR79923.1, ECO:0000313|Proteomes:UP000056630};
RN [1] {ECO:0000313|EMBL:KUR79923.1, ECO:0000313|Proteomes:UP000056630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR79923.1,
RC ECO:0000313|Proteomes:UP000056630};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUR79923.1}.
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DR EMBL; LLZR01000004; KUR79923.1; -; Genomic_DNA.
DR RefSeq; WP_067742688.1; NZ_KQ954286.1.
DR AlphaFoldDB; A0A124JZC2; -.
DR STRING; 1739114.AQZ50_03380; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000056630; Unassembled WGS sequence.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KUR79923.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000056630}.
FT DOMAIN 72..252
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 262..526
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 553 AA; 59625 MW; 5834AC05AB3648B4 CRC64;
MTTDYARARA LLNDPLTNRG TAFTVAERDH FGLHGLLPPH VLTLDEQIAR RRQMLESMDT
DFHRYAFLRE LQDTNEILFH AVVQSDLPHM LPLVYTPTVG EGCERFSQIF RRPRGLFLSW
PNRDRIRSIL ADPSLDRVKV IVVSDGERIL GLGDQGAGGM GIPIGKLALY TACAGFHPAE
VLPILLDVGT DNAERVNDPL YIGWHAPRVR GADYDAFVEE FVSAVDERFP DVLLQWEDFA
GKNAYDLLGR YRHRLLTFND DIQGTAATAV GTLLAAVRVT GVPLSAQRVV QYGLGAAGSG
IAEMLVQAIM AEGVDEATAR RTIWPIDRNG LILSDMADLP PQQVPLARDP ADVAGWARIG
NGRIGLEQTI AQVRPTVLIG TSGQRDAFNE GTVRLMASLT ERPVIFPLSN PVSRAEAHPA
DILRWSEGRA IVGSGSPFGT PGVTQVNNVY VFPGIGLGAI VAKAGVVTDG MFMAAARRLG
ELSEPGELGG EIGDGSAEGN PGLLPPITAL REVALQIAYA VAQQALAEGV AGVPAETITL
DAIAAQMWEP VYD
//
